ID V9GEH2_9BACL Unreviewed; 688 AA.
AC V9GEH2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=JCM10914_4658 {ECO:0000313|EMBL:GAE08367.1};
OS Paenibacillus sp. JCM 10914.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE08367.1, ECO:0000313|Proteomes:UP000018028};
RN [1] {ECO:0000313|EMBL:GAE08367.1, ECO:0000313|Proteomes:UP000018028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE08367.1,
RC ECO:0000313|Proteomes:UP000018028};
RA Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA Hattori M.;
RT "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL Genome Announc. 2:e01144-13(2014).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAE08367.1}.
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DR EMBL; BAUO01000021; GAE08367.1; -; Genomic_DNA.
DR RefSeq; WP_023964019.1; NZ_BAZR01000021.1.
DR AlphaFoldDB; V9GEH2; -.
DR STRING; 1236974.GCA_001315105_04548; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000018028; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08155; catalase_clade_2; 1.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000018028}.
FT DOMAIN 34..422
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 78
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 118
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 167
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 364
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 368
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-2"
FT BINDING 375
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 688 AA; 77225 MW; 734C37C26C74768F CRC64;
MDKSNANPNN KKNKTSKDQQ LEQFTVDNDG THMTTNQGLK VSEDEFSLKA GERGPTLMED
FHFREKMTHF DHERIPERIV HARGFGAHGY FQVYESMKEY TSAAFLQDPS IQTPVFVRFS
TVAGSRGSAD TVRDVRGFAA KFYTEEGNYD LVGNNMPVFF IQDAMKFPDF IHAVKPEPHN
EIPQAQSAHD TFWDFVVNNT ETAHMVMWAM SDRSLPRSFR MMEGFGVHTF RFVNDEGKAH
FIKFHWKPVL GVHSLVWDET QKLAGKDPDF NRRDLWDAIE SGNYPEYEFG VQMIAEDEEF
NFDFDILDPT KVWPEEMIPV KIIGKMTLNR NTDNFFAETE QIAFHPGHVV PGIDFTNDPL
LQGRLFSYTD TQLSRLGGPN FHEIPINRSV SPVHNNQRDG IHRMTINKGP VSYHKNGIAG
NTPKPVPREQ GGYEHYTEKV EGRKVRARSD SFKDHYSQAA MFWNSMSEVE QQHIVAAFQF
ELGKLERKEI RQQVVDMFAN VNSELAKRIS DGIGTIPPQS AGSASTESSP ALSMMNTIKS
TATRKVAVIA ANGYTDELPI IIEQLKQADL TVEIVSVKLG MIRGESSGES EVKHALLGAD
SVLFDAVLIV GGSSSISELK SEPKTVDFIK EAYQHLKPIG AIGEGANLLP AANGEGIVVV
KEGGDMKTFA HSFIDAIAAH RHWTRTVS
//
